Characterization of Phosphoenolpyruvate Carboxylase from Oceanimonas smirnovii in Escherichia coli

被引：0
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作者：
Soohyun Park
Wangjun Lee
Hyeonsoo Kim
Seung Pil Pack
Jinwon Lee
机构：
[1] Sogang University,Department of Chemical and Biomolecular Engineering
[2] Korea University,Department of Biotechnology and Bioinformatics
来源：
Applied Biochemistry and Biotechnology | 2015年 / 177卷
关键词：
Phosphoenolpyruvate carboxylase; Characterization; Bicarbonate;
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摘要：
In this study, phosphoenolpyruvate carboxylase (PEPC) derived from Oceanimonas smirnovii (OS) was expressed as a soluble protein in Escherichia coli BL21(DE3). We isolated OS-PEPC (a recombinant PEPC protein) by his-tag purification. The purified protein showed a single band upon analysis with SDS-PAGE, and it had an apparent molecular mass of 98 kDa. Pufied OS-PEPC showed a specific activity value of 21.8 ± 0.495 U/mg protein. Especially, OS-PEPC showed the enzymatic activity between 40 and 50 °C. It maintained enzymatic activity in basic pH conditions (pH value, 9–10). We also measured OS-PEPC PEP and HCO3− saturation kinetics and confirmed the effect of divalent cation on OS-PEPC activity.
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页码：217 / 225
页数：8
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